• Journal of environmental and Sanitary engineering
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• v.12 no.2
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• pp.59-64
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• 1997

For purification of a 70kDa toxic protein of mosquitocidal delta-endotoxin from B. thuringiensis strain H9B, immuno-affinity chromatography was performed. After separation of 70kDa toxic proteins from the delta-endotoxin of the strain H9B on SDS-PAGE, the 70kDa toxic protein was subcutaneously injected into rabbit for making a polyclonal antibody. A anti-70kDa toxic protein was purified by a column chromatography packed with protein A-sepharose 4B gels. The 70kDa toxic protein from delta-endotoxin of the strain H9B was also purified by an immuno-affinity chromatography packed with CNBr-activated sepharose 4B gels conjugated anti-70kDa toxic protein after elution with 1/10M citric acid-1/5M Na$_{2}$HPO$_{4}$ buffer(pH3.2) containing 0.5M NaCl. The 70kDa toxic protein was purified through only one step-separation system, was demonstrated by SDS-PAGE and immunoblot.

• Journal of Life Science
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• v.9 no.1
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• pp.35-39
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• 1999

Elecrophoreticl analysis of a 36 kDa protein was runned by SDS-PAGE, isoelectric focusing (IEF) and two dimensional electrophoresis pattern. Major 36 kDa and 25, 46, 48, 66 kDa protein were detected by Coomassie blue stain on SDS-PAGE. Major 36kDa protein was eluted for production of antiserum for serological analysis, IEF and two dimensional electrophoresis. Isoelectric point of 36kDa was aout pH 8.5. Two dimensional electrophoresis of eluted 36kDa showed one point on the gel. Anti-36 kDa serum made by newzilland rabbit for serological test. In ELISA, final titer of antibody was 100×{TEX}$2^5}${/TEX} : 1. Neutralize ability of serum was examined by slide agglutination test and colonization test in rat. Anti-36 kDa serum agglutinated whole cell of V. vulnificus were inhibited colonization on intestine in rat. Accordingly In this paper contain some electrophoretical analysis and serological test of a 36 kDa OMP of V. vulnificus.

• Animal cells and systems
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• v.5 no.3
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• pp.199-203
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• 2001

Sperminogen was purified from the acid extracts of boar spermatozoa and partial peptide sequence of the 34-36 kd sperminogen was determined. Acid extracts of boar spermatozoa was gel-filtered through Sephadex G-75, and the 34-36 kd sperminogen was purified by preparative SDS-PAGE. The sperminogen bands were sliced out, and 34-36 kd sperminogen were eluted from the gel fragments and was subjected to peptide sequencing. Since the amino termini were blocked for Edman degradation method, internal amino acid sequences of the eluted 34-36 kd sperminogen were obtained from CNBr-digested peptides of sperminogen. Among several bands resolved on tricine SDS-PAGE, 14, 22 and 26 kd peptides were subjected to peptide sequencing. The ana1yzed amino acid sequences of the 26 and 22 kd peptides showed high homologies with that of the zona pellucida binding protein, Sp38, and the analyzed amino acid sequence of the 14 kd peptide showed neither sequence homology nor similarity with any known proteins.

• The Korean Journal of Mycology
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• v.27 no.4 s.91
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• pp.299-303
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• 1999

Phytase(myo-inositol-hexakis phosphate 3-phosphohydrolase, E C 3.1.3.8) sequentially hydrolyzes phytate to myo-inositol and inorganic phosphate. Phytase of Aspergillus ficuum was purified to homogeneity using ultrafiltration, cation exchange column and anion exchange column. It's molecular weight is estimated as around 90,000 by SDS-PAGE. Antibody against the phytase was produced by immunizing mice with the purified phytase. The titer of the antibody was determined to be 1/25,000.

• Journal of Marine Bioscience and Biotechnology
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• v.1 no.3
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• pp.206-212
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• 2006

Supercritical carbon dioxide ($SCO_2$) extraction was investigated as a method for protein-sourcing material from squid viscera. To find the optimum conditions, the extraction of squid viscera using $SCO_2$ was performed under the conditions of temperature range from 35 to $45^{\circ}C$ and constant pressure 25 MPa using Hewlett-Packard 7680T. Also from result of SDS-PAGE, the protein denaturation was minimized when using $SCO_2$ extraction. And the major amino acids in the squid viscera were glutamic acid, aspartic acid, lysine, leucine, arginine, alanine, glycine, isoleucine, and valine. The main fatty acids from squid viscera were myristic acid, palmitic acid, stearic acid, heneicosanoic acid, palmitoleic acid, elaidic acid, oleic acid, eicosenoic acid, EPA (eicosapentaenoic acid), and DHA (docosahexaenoic acid).

• BMB Reports
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• v.33 no.6
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• pp.510-513
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• 2000

Boar sperminogen was purified from the acid extracts of the washed epididymal spermatozoa by gel filtration through a Sephadex G-100 column, followed by preparative SDS-PAGE. The 32 kDa sperminogen band was sliced out from the preparative SDS-PAGE and 32 kDa sperminogen was eluted from the gel matrix. The purified 32 kDa sperminogen was subjected to amino acid composition analysis. The amino acid composition of the 32 kDa boar sperminogen showed significant differences from that of either boar proacrosin or ${\beta}-acrosin$, which signifies that 32 kDa sperminogen might not be a breakdown product of proacrosin-acrosin system and that the 32 kDa sperminogen is a different protein from proacrosin-acrosin system.

• Journal of Sericultural and Entomological Science
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• v.38 no.1
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• pp.53-56
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• 1996

To investigate the molecular biological marker in insect cells, BmN-4 and Sf-0 cells were analysed by SDS-PAGE and random amplification of polymorphic DNA. The results showed that the patterns of total cell protein and random amplification of polymorphic DNA were distinguished between BmN-4 and Sf-9 cells, suggesting that the unique major bands were useful as molecular biological marker in BmN-4 and Sf-9 cells.

• Journal of Microbiology and Biotechnology
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• v.7 no.6
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• pp.435-437
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• 1997

The role of $Ca^{2+}$ in making functional malate synthase in Corynebacterium glutamicum was investigated using the cloned DNA coding for the enzyme. Introduction of cloned aceB into C. glutamicum overexpressed malate synthase as judged by SDS-PAGE. However, the increase in enzyme activity of the expressed malate synthase did not match the level of overexpression observed in SDS-PAGE. Addition of $Ca^{2+}$ to the growth medium specifically increased the activity. The malate synthase could be stained with ruthenium red in a $Ca^{2+}$-specific manner. This agrees with the previous observation which reported a potential $Ca^{2+}$-binding domain in the N-terminal region of the protein.

• Food Science and Biotechnology
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• v.17 no.4
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• pp.728-733
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• 2008

New gluten-free food product (tarhana) was produced using rice and com flours. Chemical and sensory properties of the tarhana samples were investigated and compared with those of traditional wheat tarhana. Generally, sensory analysis results indicated that utilization of com and rice flours in tarhana resulted in acceptable soup properties in terms of some of the sensory properties. The changes in electrophoretic properties of the proteins of the tarhana samples were also studied during the tarhana production. Sodium dodecyl sulfate-polyacryamide gel electrophoresis (SDS-PAGE) results showed that relative intensities of some of the protein bands in tarhana samples generally decreased during fermentation. The decrease was more obvious at the larger molecular weight region. Corn and rice tarhana seem to be promising food products for the celiac patients who have limited choice of cereal based foods.

• Microbiology and Biotechnology Letters
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• v.30 no.4
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• pp.320-324
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• 2002

To establish a rapidly immunochemical identification on a dinoflagellate, Cochlodinium polykrikoides, a specific antigenic protein as a maker on the cell membrane was isolated. The cell membranes of C. polykrikoides and Gymnodinium sangineum were harvested by centrifugation after osmotic shock. The membrane proteins of both cells were solubilized in 50 mM Na-carbonate contained 1 mM DTT, and separated the proteins on SDS-PACE. Immune-blot on the solubilized membrane proteins of the both cells was performed with antiserum against the solubilized membrane proteins of C. polykrikoides. A 120 kDa membrane protein of C. polykrikoides had remarkablely different antigenicity from that of G. sangineum.